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Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity
(Elsevier, 2015-02)
Natural β-folds manage to fold up successfully. By contrast, attempts to dissect fragments or peptides from well folded β-sheet proteins have met with insurmountable difficulties. Here we briefly review selected successful ...
Structural coalescence underlies the aggregation propensity of a β-barrel protein motif
(Public Library of Science, 2017-02)
A clear understanding of the structural foundations underlying protein aggregation is an elusive goal of central biomedical importance. A step toward this aim is exemplified by the β- barrel motif represented by the ...
Characterization of fatty acid binding and transfer from ∆98∆, a functional all-β abridged form of IFABP
(Elsevier Science, 2014-12)
Intestinal fatty acid binding protein (IFABP) is an intracellular lipid binding protein whose specific functions within the cell are still uncertain. An abbreviated version of IFABP encompassing residues 29–126, dubbed ...
Toward a common aggregation mechanism for a β-barrel protein family: insights derived from a stable dimeric species
(Elsevier Science, 2014-09)
Δ78Δ is a second generation functional all-β sheet variant of IFABP (intestinal fatty acid binding protein) corresponding to the fragment 29-106 of the parent protein. This protein and its predecessor, Δ98Δ (segment 29-126 ...
Folding of a dimeric β-barrel: Residual structure in the urea denatured state of the human papillomavirus E2 DNA binding domain
(Cambridge University Press, 2000-04)
The dimeric beta-barrel is a characteristic topology initially found in the transcriptional regulatory domain of the E2 DNA binding domain from papillomaviruses. We have previously described the kinetic folding mechanism ...
Truncation of a β-barrel scaffold dissociates intrinsic stability from its propensity to aggregation
(Cell Press, 2012-11)
Δ98Δ is a functional all-β sheet variant of intestinal fatty acid binding protein (IFABP) that was generated by controlled proteolysis. This framework is useful to study the molecular determinants related to aggregation ...
Fatty acid and retinol-binding protein: Unusual protein conformational and cavity changes dictated by ligand fluctuations
(American Chemical Society, 2019-07-31)
Lipid-binding proteins (LBPs) are soluble proteins responsible for the uptake, transport, and storage of a large variety of hydrophobic lipophilic molecules including fatty acids, steroids, and other lipids in the cellular ...
The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding
(American Society For Biochemistry And Molecular Biology, 2011)
Cerato-platanin (CP) is a secretion protein produced by the fungal pathogen Ceratocystis platani, the causal agent of the plane canker disease and the first member of the CP family. CP is considered a pathogen-associated ...
Conformational changes, from β-strand to α-helix, of the fatty acid-binding protein ReP1-NCXSQ in anionic lipid membranes: dependence with the vesicle curvature
(Springer, 2017-07)
We studied the conformational changes of the fatty acid-binding protein ReP1-NCXSQ in the interface of anionic lipid membranes. ReP1-NCXSQ is an acidic protein that regulates the activity of the Na+/Ca2+ exchanger in squid ...
Kinetics and Thermodynamics of Membrane Protein Folding
(Molecular Diversity Preservation International, 2014-03)
Understanding protein folding has been one of the great challenges in biochemistry and molecular biophysics. Over the past 50 years, many thermodynamic and kinetic studies have been performed addressing the stability of ...